Biochemical and molecular properties of the cytochrome P450 arachidonic acid monooxygenases

Jorge H. Capdevila, J R Falck

Research output: Contribution to journalArticle

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Abstract

The cytochrome P450 (P450) arachidonic acid (AA) monooxygenase metabolizes the fatty acid to a series of epoxy- and hydroxy-acid derivatives. Catalytic turnover requires NADPH, and requires the redox-coupled activation and cleavage of diatomic oxygen, and the delivery of an active form of atomic oxygen to ground state carbon atoms. Past and present advances in P450 biochemistry and molecular biology are beginning to provide a description of the P450 isoform specificity of AA bioactivation, and the mechanisms of action and physiological relevance of the P450 metabolites. The demonstration of the endogenous biosynthesis of many of these metabolites has established the P450 pathway as an important route for AA bioactivation, and has begun to uncovered new and important functional roles for this enzyme system in cell and organ physiology.

Original languageEnglish (US)
Pages (from-to)325-344
Number of pages20
JournalProstaglandins and Other Lipid Mediators
Volume68-69
DOIs
StatePublished - Aug 1 2002

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Keywords

  • Arachidonic acid bioactivation
  • Cytochrome P450
  • Physiological role

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Pharmacology
  • Cell Biology

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